دورية أكاديمية

Kinetics and energetics of the translocation of maltose binding protein folding mutants.

التفاصيل البيبلوغرافية
العنوان: Kinetics and energetics of the translocation of maltose binding protein folding mutants.
المؤلفون: Tomkiewicz D; Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands., Nouwen N, Driessen AJ
المصدر: Journal of molecular biology [J Mol Biol] 2008 Mar 14; Vol. 377 (1), pp. 83-90. Date of Electronic Publication: 2008 Jan 15.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1089-8638 (Electronic) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: 1959- : London : Academic Press
مواضيع طبية MeSH: Protein Folding*, Escherichia coli/*metabolism , Escherichia coli Proteins/*chemistry , Escherichia coli Proteins/*metabolism , Mutant Proteins/*chemistry , Mutant Proteins/*metabolism , Mutation/*genetics , Periplasmic Binding Proteins/*chemistry , Periplasmic Binding Proteins/*metabolism, Adenosine Triphosphatases/metabolism ; Bacterial Proteins/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/isolation & purification ; Carrier Proteins/metabolism ; Endopeptidase K/metabolism ; Escherichia coli Proteins/isolation & purification ; Kinetics ; Membrane Transport Proteins/metabolism ; Mutagenesis ; Mutant Proteins/isolation & purification ; Periplasmic Binding Proteins/isolation & purification ; Protein Precursors/chemistry ; Protein Precursors/isolation & purification ; Protein Precursors/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; SEC Translocation Channels ; SecA Proteins ; Spectrometry, Fluorescence ; Thermodynamics ; Tryptophan
مستخلص: Protein translocation in Escherichia coli is mediated by the translocase that, in its minimal form, comprises a protein-conducting pore (SecYEG) and a motor protein (SecA). The SecYEG complex forms a narrow channel in the membrane that allows passage of secretory proteins (preproteins) in an unfolded state only. It has been suggested that the SecA requirement for translocation depends on the folding stability of the mature preprotein domain. Here we studied the effects of the signal sequence and SecB on the folding and translocation of folding stabilizing and destabilizing mutants of the mature maltose binding protein (MBP). Although the mutations affect the folding of the precursor form of MBP, these are drastically overruled by the combined unfolding stabilization of the signal sequence and SecB. Consequently, the translocation kinetics, the energetics and the SecA and SecB dependence of the folding mutants are indistinguishable from those of wild-type preMBP. These data indicate that unfolding of the mature domain of preMBP is likely not a rate-determining step in translocation when the protein is targeted to the translocase via SecB.
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Carrier Proteins)
0 (Escherichia coli Proteins)
0 (MalE protein, E coli)
0 (Membrane Transport Proteins)
0 (Mutant Proteins)
0 (Periplasmic Binding Proteins)
0 (Protein Precursors)
0 (SEC Translocation Channels)
0 (preMBP protein, E coli)
8DUH1N11BX (Tryptophan)
EC 3.4.21.64 (Endopeptidase K)
EC 3.6.1.- (Adenosine Triphosphatases)
EC 7.4.2.4 (SecA Proteins)
تواريخ الأحداث: Date Created: 20080205 Date Completed: 20080324 Latest Revision: 20191210
رمز التحديث: 20231215
DOI: 10.1016/j.jmb.2008.01.014
PMID: 18241889
قاعدة البيانات: MEDLINE
الوصف
تدمد:1089-8638
DOI:10.1016/j.jmb.2008.01.014